ST6GAL1

ST6GAL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4JS1, 4JS2
Identifiers
Aliases	ST6GAL1, SIAT1, ST6GalI, ST6N, ST6 beta-galactoside alpha-2,6-sialyltransferase 1, CDw75
External IDs	OMIM: 109675 MGI: 108470 HomoloGene: 2281 GeneCards: ST6GAL1
Gene location (Human) Chr. Chromosome 3 (human) Band 3q27.3 Start 186,930,325 bp End 187,078,553 bp
Gene location (Mouse) Chr. Chromosome 16 (mouse) Band 16 B1|16 14.03 cM Start 23,043,490 bp End 23,179,100 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in liver right lobe of liver renal medulla lymph node bone marrow cells urethra bronchus bronchial epithelial cell trachea thymus Top expressed in sciatic nerve utricle iris condyle Paneth cell motor neuron primitive streak left lung lobe facial motor nucleus ascending aorta More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity glycosyltransferase activity protein binding sialyltransferase activity beta-galactoside alpha-2,6-sialyltransferase activity protein homodimerization activity Cellular component integral component of membrane Golgi apparatus membrane Golgi cisterna membrane extracellular region Golgi membrane Biological process sialylation protein glycosylation humoral immune response O-glycan processing oligosaccharide metabolic process N-acetylneuraminate metabolic process protein N-linked glycosylation via asparagine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6480 20440 Ensembl ENSG00000073849 ENSMUSG00000022885 UniProt P15907 Q64685 RefSeq (mRNA) NM_003032 NM_173216 NM_173217 NM_001353916 NM_001252505 NM_001252506 NM_145933 RefSeq (protein) NP_003023 NP_775323 NP_775324 NP_001340845 NP_001239434 NP_001239435 NP_666045 Location (UCSC) Chr 3: 186.93 – 187.08 Mb Chr 16: 23.04 – 23.18 Mb PubMed search
Wikidata
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Beta-galactoside alpha-2,6-sialyltransferase 1 is an enzyme that in humans is encoded by the ST6GAL1 gene.

The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein, which is normally found in the Golgi but which can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CDw75, and CD76. This protein is a member of glycosyltransferase family 29. Three transcript variants encoding two different isoforms have been found for this gene.

Transcripts of ST6GAL1 are found in mouse high endothelial cells of mesenteric lymph node and Peyer's patches, and it could be involved in the B cell homing to Peyer's patches. ST6GAL1 expression has also shown to be upregulated in several types of cancers and has been shown to haves roles in cancer survival and metastasis.

Further reading

• Bast BJ, Zhou LJ, Freeman GJ, et al. (1992). "The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface carbohydrate determinants generated by the beta-galactoside alpha 2,6-sialyltransferase". J. Cell Biol. 116 (2): 423–35. doi:10.1083/jcb.116.2.423. PMC 2289289. PMID 1730763.
• Stamenkovic I, Asheim HC, Deggerdal A, et al. (1990). "The B cell antigen CD75 is a cell surface sialytransferase". J. Exp. Med. 172 (2): 641–3. doi:10.1084/jem.172.2.641. PMC 2188328. PMID 2373995.
• Lance P, Lau KM, Lau JT (1989). "Isolation and characterization of a partial cDNA for a human sialyltransferase". Biochem. Biophys. Res. Commun. 164 (1): 225–32. doi:10.1016/0006-291X(89)91706-3. PMID 2803295.
• Rabouille C, Hui N, Hunte F, et al. (1995). "Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides". J. Cell Sci. 108. ( Pt 4) (4): 1617–27. doi:10.1242/jcs.108.4.1617. PMID 7615680.
• Bruneau N, Lombardo D (1995). "Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase". J. Biol. Chem. 270 (22): 13524–33. doi:10.1074/jbc.270.22.13524. PMID 7768954.
• Wang X, Vertino A, Eddy RL, et al. (1993). "Chromosome mapping and organization of the human beta-galactoside alpha 2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells". J. Biol. Chem. 268 (6): 4355–61. doi:10.1016/S0021-9258(18)53617-6. PMID 7786324.
• Hanasaki K, Varki A, Stamenkovic I, Bevilacqua MP (1994). "Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands". J. Biol. Chem. 269 (14): 10637–43. doi:10.1016/S0021-9258(17)34107-8. PMID 8144653.
• Aasheim HC, Aas-Eng DA, Deggerdal A, et al. (1993). "Cell-specific expression of human beta-galactoside alpha 2,6-sialyltransferase transcripts differing in the 5' untranslated region". Eur. J. Biochem. 213 (1): 467–75. doi:10.1111/j.1432-1033.1993.tb17783.x. PMID 8477718.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Sgroi D, Nocks A, Stamenkovic I (1996). "A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33". J. Biol. Chem. 271 (31): 18803–9. doi:10.1074/jbc.271.31.18803. PMID 8702538.
• Lo NW, Lau JT (1996). "Transcription of the beta-galactoside alpha 2,6-sialyltransferase gene in B lymphocytes is directed by a separate and distinct promoter". Glycobiology. 6 (3): 271–9. doi:10.1093/glycob/6.3.271. PMID 8724135.
• Lo NW, Lau JT (1996). "Novel heterogeneity exists in the 5'-untranslated region of the beta-galactoside alpha 2,6-sialytransferase mRNAs in the human B-lymphoblastoid cell line, louckes". Biochem. Biophys. Res. Commun. 228 (2): 380–5. doi:10.1006/bbrc.1996.1670. PMID 8920923.
• Tsuji S, Datta AK, Paulson JC (1997). "Systematic nomenclature for sialyltransferases". Glycobiology. 6 (7): v–vii. doi:10.1093/glycob/6.7.647. PMID 8953271.
• Ma J, Qian R, Rausa FM, Colley KJ (1997). "Two naturally occurring alpha2,6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing". J. Biol. Chem. 272 (1): 672–9. doi:10.1074/jbc.272.1.672. PMID 8995311.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Lo NW, Lau JT (1999). "Transcription of the beta-galactoside alpha2,6-sialyltransferase gene (SIAT1) in B-lymphocytes: cell type-specific expression correlates with presence of the divergent 5'-untranslated sequence". Glycobiology. 9 (9): 907–14. doi:10.1093/glycob/9.9.907. PMID 10460832.
• Laroy W, Ameloot P, Contreras R (2001). "Characterization of sialyltransferase mutants using surface plasmon resonance". Glycobiology. 11 (3): 175–82. doi:10.1093/glycob/11.3.175. PMID 11320056.
• Qian R, Chen C, Colley KJ (2001). "Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing". J. Biol. Chem. 276 (31): 28641–9. doi:10.1074/jbc.M103664200. PMID 11356854.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37 (2): 210–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.